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Am J Physiol Gastrointest Liver Physiol 282: G375-G381, 2002; doi:10.1152/ajpgi.00386.2001
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Vol. 282, Issue 2, G375-G381, February 2002

Cloning of human agmatinase. An alternate path for polyamine synthesis induced in liver by hepatitis B virus

Sanjay K. Mistry1, Tim J. Burwell2, Rebecca M. Chambers2, Laura Rudolph-Owen2, Frank Spaltmann3, W. Jim Cook2, and Sidney M. Morris Jr1

1 Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261; 2 Millennium Pharmaceuticals, Cambridge, Massachusetts 02139; and 3 Bayer, West Haven, Connecticut 06516 - 4175

Agmatinase, which hydrolyzes agmatine to putrescine and urea, not only represents a potentially important mechanism for regulating the biological effects of agmatine in mammalian cells but also represents an alternative to ornithine decarboxylase for polyamine biosynthesis. We have isolated a full-length cDNA encoding human agmatinase whose function was confirmed by complementation in yeast. The single-copy human agmatinase gene located on chromosome 1 encodes a 352-residue protein with a putative mitochondrial targeting sequence at the NH3-terminus. Human agmatinase has about 30% identity to bacterial agmatinases and <20% identity to mammalian arginases. Residues required for binding of Mn2+ at the active site in bacterial agmatinase and other members of the arginase superfamily are fully conserved in human agmatinase. Agmatinase mRNA is most abundant in human liver and kidney but also is expressed in several other tissues, including skeletal muscle and brain. Its expression in human liver is induced during hepatitis B virus infection, suggesting that agmatinase may play a role in the pathophysiology of this disease.

brain; kidney; putrescine; arginase superfamily


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